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Does Bromodomain Flexibility Influence Histone Recognition?

Does Bromodomain Flexibility Influence Histone Recognition?

Sandra Steiner, Andrea Magno, Danzhi Huang, Amedeo Caflisch

FEBS Lett. 2013 Jul 11;587(14):2158-63.

PMID: 23711371

Abstract:

Bromodomains are protein modules that selectively recognize histones by binding to acetylated lysines. Here, we have carried out multiple molecular dynamics simulations of 20 human bromodomains to investigate the flexibility of their binding site. Some bromodomains show alternative side chain orientations of three evolutionarily conserved residues: the Asn involved in acetyl-lysine binding and two conserved aromatic residues. Furthermore, for the BAZ2B and CREBBP bromodomains we observe occlusion of the binding site which is coupled to the displacement of the two aromatic residues. In contrast to available structures, the simulations reveal large variability of the binding site accessibility. The simulations suggest that the flexibility of the bromodomain binding site and presence of self-occluded metastable states influence the recognition of acetyl-lysine on histone tails.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416126	ATAD2B (953-1080) human			Price

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